Research workbench
Correlated disorder of the pure PRO22(SLASH)LEU25 form of crambin at 150K refined to 1.05 ångströms resolution
Analyse Correlated disorder of the pure PRO22(SLASH)LEU25 form of crambin at 150K… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CNR
- Type
- protein
- Length
- 46 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Crambin
- UniProt
- P01542
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Crambin | protein | 46 | 48% helix, 9% strand | P01542 |
Ligands and binding sites
- EOH · Ethanol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1CNR · Correlated disorder of the pure PRO22(SLASH)LEU25 form of crambin at 150K refined to 1.05… · the same entry in another collection · chain A against A, TM-score 1.00
- P01542 · AlphaFold monomer V2.0 prediction for crambin (P01542) · a predicted model of the same protein · chain A against A, TM-score 0.95
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P01542
- Elsewhere: RCSB PDB 1CNR · PDBe 1CNR · UniProt P01542
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